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How PROTAC Degraders Work: Molecular Recognition and Design Principles

30 Jul 21

Speaker: Alessio Ciulli, PhD - Professor of Chemical & Structural Biology - School of Life Sciences, Division of Biological Chemistry and Drug Discovery, University of Dundee



Organizer: IRB Barcelona

Date: Friday  30 July 2021, 12.00h

Title: How PROTAC Degraders Work: Molecular Recognition and Design Principles

Host: Cristina Mayor-Ruiz, PhD - GL Targeted protein degradation and drug discovery Lab

Biomed Webinar



Proteolysis-targeting chimeras (PROTACs) are a new class of chemical tools and drugs that target disease-causing proteins for degradation. They are designed to harness the cell’s natural disposal system (the ubiquitin-proteasome) to specifically remove proteins. A PROTAC is a two-headed (i.e. bifunctional) molecule where one end binds an enzyme (an E3 ubiquitin ligase) and the other binds the target protein, bringing the two proteins into close proximity as a ternary complex. The ligase is then able to label the target protein for ubiquitination and so degradation by the cell’s disposal system. Whereas conventional drugs only inhibit disease proteins by binding and locking up their most important functional parts for the duration of the drug's action, PROTACs can bind at any positions and rapidly cause the disease protein’s permanent and long-lasting destruction. Due to this revolutionary mode of action, PROTACs can attack targets previously thought ‘undruggable’. In this lecture, I will outline some key discoveries from my laboratory that have advanced the chemistry and structural biology of PROTACs, and are providing fundamental insights into our understanding of their molecular recognition, mechanism of action and drug design. 


Open to predoctoral UPF students

If you are interested in participating please send an email to